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Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome
- Source :
- Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual), Universidade de São Paulo (USP), instacron:USP
- Publication Year :
- 2017
-
Abstract
- The p23 proteins are small acidic proteins that aid the functional cycle of the Hsp90 molecular chaperone. Such co-chaperone acts by temporarily inhibiting the ATPase activity of Hsp90 and exhibits intrinsic chaperone activity, suggesting independent roles. A search for p23 in the Plasmodium falciparum genome led to the identification of two putative proteins showing 13% identity to each other and approximately 20% identity to human p23. To understand the presence of two p23 proteins in this organism, we generated recombinant p23 proteins (Pfp23A and Pfp23B) and investigated their structure and function. The proteins presented some similarities and dissimilarities in structural contents and showed different chemical and thermal stabilities, with Pfp23A being more stable than Pfp23B, suggesting that these proteins may present different functions in this organism. Both Pfp23 proteins behaved as elongated monomers in solution and were capable of preventing the thermal-induced aggregation of model client proteins with different efficiencies. Finally, the Pfp23 proteins inhibited the ATPase activity of recombinant P. falciparum Hsp90 (PfHsp90). These results validate the studied proteins as p23 proteins and co-chaperones of PfHsp90.
- Subjects :
- 0301 basic medicine
Models, Molecular
congenital, hereditary, and neonatal diseases and abnormalities
Protein Conformation
Plasmodium falciparum
Gene Expression
Biochemistry
Genome
law.invention
03 medical and health sciences
chemistry.chemical_compound
Structure-Activity Relationship
Structural Biology
law
BIOQUÍMICA CELULAR
Amino Acid Sequence
HSP90 Heat-Shock Proteins
Chaperone activity
skin and connective tissue diseases
Molecular Biology
Organism
030102 biochemistry & molecular biology
biology
Protein Stability
Low resolution
Hydrolysis
General Medicine
Sequence Analysis, DNA
biology.organism_classification
Hsp90
Recombinant Proteins
DNA-Binding Proteins
030104 developmental biology
Monomer
chemistry
Solubility
biology.protein
Recombinant DNA
Genome, Protozoan
Molecular Chaperones
Subjects
Details
- ISSN :
- 18790003
- Volume :
- 108
- Database :
- OpenAIRE
- Journal :
- International journal of biological macromolecules
- Accession number :
- edsair.doi.dedup.....709ad268088e5e5baef7dddf50161600